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Protein

Anaphase-promoting complex subunit cut9

Gene

cut9

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. May play a pivotal role in the control of anaphase.1 Publication

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • positive regulation of mitotic metaphase/anaphase transition Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Anaphase-promoting complex subunit cut9
Alternative name(s):
20S cyclosome/APC complex protein cut9
Cell untimely torn protein 9
Gene namesi
Name:cut9
Synonyms:dre1
ORF Names:SPAC6F12.15c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC6F12.15c.
PomBaseiSPAC6F12.15c. cut9.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: PomBase
  • cytosol Source: PomBase
  • nuclear pericentric heterochromatin Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi412 – 4121G → D in cut9-T98; temperature-sensitive. 1 Publication
Mutagenesisi535 – 5351A → T in cut9-665; temperature-sensitive. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671Anaphase-promoting complex subunit cut9PRO_0000106281Add
BLAST

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41889.

Interactioni

Subunit structurei

The APC/C is composed of at least 13 subunits: apc1, apc2, nuc2, apc4, apc5, cut9, apc8, apc10, apc11, hcn1, apc13, apc14 and apc15. Homodimer. Interacts directly with nuc2 and hcn1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
apc14O426592EBI-1160859,EBI-1251592
apc15O946882EBI-1160859,EBI-1251604
hcn1O139162EBI-1160859,EBI-1251563

Protein-protein interaction databases

BioGridi278089. 47 interactions.
IntActiP41889. 6 interactions.
MINTiMINT-4690227.

Structurei

Secondary structure

1
671
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 534Combined sources
Helixi55 – 595Combined sources
Helixi83 – 9614Combined sources
Helixi100 – 11415Combined sources
Helixi117 – 12913Combined sources
Helixi133 – 14210Combined sources
Helixi145 – 1473Combined sources
Helixi150 – 16213Combined sources
Helixi166 – 1738Combined sources
Helixi198 – 21215Combined sources
Helixi216 – 22914Combined sources
Helixi234 – 2429Combined sources
Helixi248 – 25710Combined sources
Helixi261 – 2644Combined sources
Helixi265 – 2673Combined sources
Helixi268 – 2769Combined sources
Turni281 – 2844Combined sources
Helixi285 – 29612Combined sources
Helixi301 – 3033Combined sources
Helixi305 – 31713Combined sources
Helixi321 – 33414Combined sources
Helixi342 – 35211Combined sources
Helixi355 – 36814Combined sources
Helixi373 – 38513Combined sources
Helixi389 – 40214Combined sources
Helixi407 – 42014Combined sources
Helixi423 – 43513Combined sources
Turni436 – 4394Combined sources
Helixi442 – 45413Combined sources
Helixi457 – 47014Combined sources
Helixi475 – 48713Combined sources
Helixi491 – 50717Combined sources
Helixi513 – 5153Combined sources
Helixi516 – 52813Combined sources
Helixi532 – 54514Combined sources
Helixi550 – 56213Combined sources
Helixi566 – 57914Combined sources
Helixi584 – 5929Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XPIX-ray2.60A/D1-597[»]
ProteinModelPortaliP41889.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati83 – 11432TPR 1Add
BLAST
Repeati117 – 14226TPR 2Add
BLAST
Repeati150 – 17324TPR 3Add
BLAST
Repeati198 – 22932TPR 4Add
BLAST
Repeati234 – 25724TPR 5Add
BLAST
Repeati268 – 29629TPR 6Add
BLAST
Repeati306 – 33429TPR 7Add
BLAST
Repeati341 – 36828TPR 8Add
BLAST
Repeati373 – 40230TPR 9Add
BLAST
Repeati407 – 43529TPR 10Add
BLAST
Repeati442 – 47029TPR 11Add
BLAST
Repeati475 – 50733TPR 12Add
BLAST
Repeati513 – 54533TPR 13Add
BLAST
Repeati550 – 57930TPR 14Add
BLAST

Domaini

TPR repeats 1-7 mediate homodimerization while TPR repeats 8 and 10-13 bind to hcn1, burying its N-terminal acetyl-methionine.1 Publication

Sequence similaritiesi

Contains 14 TPR repeats.PROSITE-ProRule annotation1 Publication

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

HOGENOMiHOG000160791.
InParanoidiP41889.
KOiK03353.
OMAiFIDMRRY.
OrthoDBiEOG7ZKSKQ.
PhylomeDBiP41889.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41889-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVKRTQTDS RMQSTPGNHN HPDAHANAAY MTPPSMGALN ANNSNSQLST
60 70 80 90 100
LTISPMTYLA NNTSTDGSFL KERNAQNTDS LSREDYLRLW RHDALMQQQY
110 120 130 140 150
KCAAFVGEKV LDITGNPNDA FWLAQVYCCT GDYARAKCLL TKEDLYNRSS
160 170 180 190 200
ACRYLAAFCL VKLYDWQGAL NLLGETNPFR KDEKNANKLL MQDGGIKLEA
210 220 230 240 250
SMCYLRGQVY TNLSNFDRAK ECYKEALMVD AKCYEAFDQL VSNHLLTADE
260 270 280 290 300
EWDLVLKLNY STYSKEDAAF LRSLYMLKLN KTSHEDELRR AEDYLSSING
310 320 330 340 350
LEKSSDLLLC KADTLFVRSR FIDVLAITTK ILEIDPYNLD VYPLHLASLH
360 370 380 390 400
ESGEKNKLYL ISNDLVDRHP EKAVTWLAVG IYYLCVNKIS EARRYFSKSS
410 420 430 440 450
TMDPQFGPAW IGFAHSFAIE GEHDQAISAY TTAARLFQGT HLPYLFLGMQ
460 470 480 490 500
HMQLGNILLA NEYLQSSYAL FQYDPLLLNE LGVVAFNKSD MQTAINHFQN
510 520 530 540 550
ALLLVKKTQS NEKPWAATWA NLGHAYRKLK MYDAAIDALN QGLLLSTNDA
560 570 580 590 600
NVHTAIALVY LHKKIPGLAI THLHESLAIS PNEIMASDLL KRALEENSLT
610 620 630 640 650
SGFLNSKYVF EDEVSEYMQQ SNLNTSDKSM SMEDQSGKVT ESVNDRTQVL
660 670
YADSRSEMMM DDIEGNVSEQ R
Length:671
Mass (Da):75,889
Last modified:July 15, 1998 - v2
Checksum:i5300382396270BE2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031A → C (PubMed:7798319).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31844 Genomic DNA. Translation: BAA06630.1.
CU329670 Genomic DNA. Translation: CAB11098.1.
PIRiA55164.
RefSeqiNP_593301.1. NM_001018731.2.

Genome annotation databases

EnsemblFungiiSPAC6F12.15c.1; SPAC6F12.15c.1:pep; SPAC6F12.15c.
GeneIDi2541592.
KEGGispo:SPAC6F12.15c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31844 Genomic DNA. Translation: BAA06630.1.
CU329670 Genomic DNA. Translation: CAB11098.1.
PIRiA55164.
RefSeqiNP_593301.1. NM_001018731.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XPIX-ray2.60A/D1-597[»]
ProteinModelPortaliP41889.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278089. 47 interactions.
IntActiP41889. 6 interactions.
MINTiMINT-4690227.

Proteomic databases

MaxQBiP41889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC6F12.15c.1; SPAC6F12.15c.1:pep; SPAC6F12.15c.
GeneIDi2541592.
KEGGispo:SPAC6F12.15c.

Organism-specific databases

EuPathDBiFungiDB:SPAC6F12.15c.
PomBaseiSPAC6F12.15c. cut9.

Phylogenomic databases

HOGENOMiHOG000160791.
InParanoidiP41889.
KOiK03353.
OMAiFIDMRRY.
OrthoDBiEOG7ZKSKQ.
PhylomeDBiP41889.

Miscellaneous databases

PROiP41889.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bypassing anaphase by fission yeast cut9 mutation: requirement of cut9+ to initiate anaphase."
    Samejima I., Yanagida M.
    J. Cell Biol. 127:1655-1670(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-412 AND ALA-535.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Distinct subunit functions and cell cycle regulated phosphorylation of 20S APC/cyclosome required for anaphase in fission yeast."
    Yamada H., Kumada K., Yanagida M.
    J. Cell Sci. 110:1793-1804(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NUC2, PHOSPHORYLATION.
  4. "Proteomics analysis identifies new components of the fission and budding yeast anaphase-promoting complexes."
    Yoon H.-J., Feoktistova A., Wolfe B.A., Jennings J.L., Link A.J., Gould K.L.
    Curr. Biol. 12:2048-2054(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  5. "The APC/C subunit Cdc16/Cut9 is a contiguous tetratricopeptide repeat superhelix with a homo-dimer interface similar to Cdc27."
    Zhang Z., Kulkarni K., Hanrahan S.J., Thompson A.J., Barford D.
    EMBO J. 29:3733-3744(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-597 IN COMPLEX WITH HCN1, TPR REPEATS, SUBUNIT.

Entry informationi

Entry nameiCUT9_SCHPO
AccessioniPrimary (citable) accession number: P41889
Secondary accession number(s): O14231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 15, 1998
Last modified: June 8, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.